ArticleProtein science : a publication of the Protein Society1997
Refined structures of three crystal forms of toxic shock syndrome toxin-1 and of a tetramutant with reduced activity.
Article in Protein science : a publication of the Protein Society, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 28 citations in OpenAlex.
- Article
- Gram-positive bacterial superantigen outside-in signaling causes toxic shock syndrome.The FEBS journal · 2011Review
- Structural basis of T-cell specificity and activation by the bacterial superantigen TSST-1.The EMBO journal · 2007Article
- STRALCP--structure alignment-based clustering of proteins.Nucleic acids research · 2007Article
- Overview of protein structural and functional folds.Current protocols in protein science · 2004Review
- Identification of a transcytosis epitope on staphylococcal enterotoxins.Infection and immunity · 2002Article
- Exotoxins of Staphylococcus aureus.Clinical microbiology reviews · 2000Review
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8 authors at 2 institutions in 1 country.
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Abstract
The structure of toxic shock syndrome toxin-1 (TSST-1), the causative agent in toxic shock syndrome, has been determined in three crystal forms. The three structural models have been refined to R-factors of 0.154, 0.150, and 0.198 at resolutions of 2.05 A, 2.90 A, and 2.75 A, respectively. One crystal form of TSST-1 contains a zinc ion bound between two symmetry-related molecules. Although not required for biological activity, zinc dramatically potentiates the mitogenicity of TSST-1 at very low concentrations. In addition, the structure of the tetramutant TSST-1H [T69I, Y80W, E132K, I140T], which is nonmitogenic and does not amplify endotoxin shock, has been determined and refined in a fourth crystal form (R-factor = 0.173 to 1.9 A resolution).
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